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Various AKIP1 expression levels affect its subcellular localization but have no effect on NF-kappaB activation

A. Keprová, L. Kořínková, I. Křížová, R. Hadravová, F. Kaufman, I. Pichová, T. Ruml, M. Rumlová

. 2019 ; 68 (3) : 431-443. [pub] 20190322

Language English Country Czech Republic

Document type Journal Article

Persistent link   https://www.medvik.cz/link/bmc19043779

A-kinase interacting protein 1 (AKIP1) has been shown to interact with a broad range of proteins involved in various cellular processes, including apoptosis, tumorigenesis, and oxidative stress suggesting it might have multiple cellular functions. In this study, we used an epitope-tagged AKIP1 and by combination of immunochemical approaches, microscopic methods and reporter assays we studied its properties. Here, we show that various levels of AKIP1 overexpression in HEK-293 cells affected not only its subcellular localization but also resulted in aggregation. While highly expressed AKIP1 accumulated in electron-dense aggregates both in the nucleus and cytosol, low expression of AKIP1 resulted in its localization within the nucleus as a free, non-aggregated protein. Even though AKIP1 was shown to interact with p65 subunit of NF-kappaB and activate this transcription factor, we did not observe any effect on NF-kappaB activation regardless of various AKIP1 expression level.

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